eF-site ID 1ekm-B PDB Code 1ekm Chain B click to enlarge Title CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI Classification OXIDOREDUCTASE Compound COPPER AMINE OXIDASE Source null (AMO_PICAN) Sequence B:  APARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTL REPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLV DLASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIE QCVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVY YRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVS KHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTG NVMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRI SLSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGC DCKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKH SDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQD GAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNH QHLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGN AFYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSG KPPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYK DNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILF FHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLD IQPSYAMTTSEAKRAV Description (1)  COPPER AMINE OXIDASE (E.C.1.4.3.6) Functional site 1) chain B residue 405 type sequence Y description BINDING SITE FOR RESIDUE ZN B 701 source : AC2 2) chain B residue 456 type sequence H description BINDING SITE FOR RESIDUE ZN B 701 source : AC2 3) chain B residue 458 type sequence H description BINDING SITE FOR RESIDUE ZN B 701 source : AC2 4) chain B residue 624 type sequence H description BINDING SITE FOR RESIDUE ZN B 701 source : AC2 5) chain B residue 319 type ACT_SITE sequence D description Proton acceptor => ECO:0000269|PubMed:9551552 source Swiss-Prot : SWS_FT_FI1 6) chain B residue 405 type ACT_SITE sequence Y description Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI2 7) chain B residue 317 type BINDING sequence A description BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5 source Swiss-Prot : SWS_FT_FI3 8) chain B residue 402 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P46883 source Swiss-Prot : SWS_FT_FI4 9) chain B residue 456 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 10) chain B residue 458 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 11) chain B residue 624 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF source Swiss-Prot : SWS_FT_FI5 12) chain B residue 465 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 13) chain B residue 613 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 14) chain B residue 614 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:Q43077 source Swiss-Prot : SWS_FT_FI6 15) chain B residue 405 type MOD_RES sequence Y description 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE source Swiss-Prot : SWS_FT_FI7 16) chain B residue 243 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552 source Swiss-Prot : SWS_FT_FI8

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